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Literature summary for 1.1.1.95 extracted from

  • Unterlass, J.E.; Wood, R.J.; Basle, A.; Tucker, J.; Cano, C.; Noble, M.M.E.; Curtin, N.J.
    Structural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH) (2017), Oncotarget, 8, 104478-104491 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.95

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapour diffusion method, cocrystal structure of catalytic subunit of the enzyme (PHGDHs) with NAD+ and L-tartrate reveals a domain movement upon substrate binding Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
adenosine 5'-diphosphoribose 0.12 mM, 50% inhibition. NAD+ competitive inhibitor Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0053
-
 NAD+ pH 7.5, temperature not specified in the publication Homo sapiens
0.0118
-
 Thionicotinamide pH 7.5, temperature not specified in the publication Homo sapiens
0.0393
-
 acetylpyridine pH 7.5, temperature not specified in the publication Homo sapiens
0.1477
-
 pyridinealdehyde adenine dinucleotide pH 7.5, temperature not specified in the publication Homo sapiens
0.187
-
 3-phospho-D-glycerate pH 7.5, temperature not specified in the publication Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-phospho-D-glycerate + NAD+ Homo sapiens
-
 3-phosphooxypyruvate + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Homo sapiens O43175
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phospho-D-glycerate + NAD+
-
 Homo sapiens 3-phosphooxypyruvate + NADH + H+
-
 r
3-phospho-D-glycerate + NAD+ the enzyme has a 400fold higher affinity for NADH than NAD+ Homo sapiens 3-phosphooxypyruvate + NADH + H+
-
 r
3-phosphooxypyruvate + acetylpyridine
-
 Homo sapiens 3-phospho-D-glycerate + ?
-
 r
3-phosphooxypyruvate + NADH + H+ the enzyme has a 400fold higher affinity for NADH than NAD+ Homo sapiens 3-phospho-D-glycerate + NAD+
-
 r
3-phosphooxypyruvate + pyridinealdehyde adenine dinucleotide
-
 Homo sapiens 3-phospho-D-glycerate + ?
-
 r
3-phosphooxypyruvate + thionicotinamide
-
 Homo sapiens 3-phospho-D-glycerate + ?
-
 r

Subunits

Subunits Comment Organism
dimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
3-phosphoglycerate dehydrogenase
-
 Homo sapiens
Phgdh
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0035
-
 pyridinealdehyde adenine dinucleotide pH 7.5, temperature not specified in the publication Homo sapiens
0.005
-
 NAD+ pH 7.5, temperature not specified in the publication Homo sapiens
0.0075
-
 Thionicotinamide pH 7.5, temperature not specified in the publication Homo sapiens
0.017
-
 acetylpyridine pH 7.5, temperature not specified in the publication Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Homo sapiens
NADH
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the first step in the de novo synthesis pathway of serine, a critical amino acid for protein and nucleic acid biosynthesis Homo sapiens